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Protein

Fructose-1,6-bisphosphatase 1

Gene

FBP1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain (By similarity).By similarity

Catalytic activityi

D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.

Cofactori

Mg2+4 PublicationsNote: Binds 3 Mg2+ ions per subunit.4 Publications

Enzyme regulationi

Subject to complex allosteric regulation. The enzyme can assume an active R-state, or an inactive T-state. Intermediate conformations may exist. AMP acts as allosteric inhibitor. AMP binding affects the turnover of bound substrate and not the affinity for substrate. Fructose 2,6-bisphosphate acts as competitive inhibitor. Fructose 2,6-bisphosphate and AMP have synergistic effects.6 Publications

Kineticsi

  1. KM=1.2 µM for fructose-1,6-diphosphate1 Publication

    Pathwayi: gluconeogenesis

    This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi69Magnesium 11 Publication1
    Metal bindingi98Magnesium 11 Publication1
    Metal bindingi98Magnesium 21 Publication1
    Metal bindingi119Magnesium 21 Publication1
    Metal bindingi119Magnesium 31 Publication1
    Metal bindingi121Magnesium 2; via carbonyl oxygen1 Publication1
    Metal bindingi122Magnesium 31 Publication1
    Binding sitei141AMP1 Publication1
    Binding sitei265Substrate1
    Metal bindingi281Magnesium 31 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi18 – 22AMP1 Publication5
    Nucleotide bindingi28 – 32AMP1 Publication5
    Nucleotide bindingi113 – 114AMP1 Publication2

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Gluconeogenesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.1.3.11. 6170.
    SABIO-RKP00636.
    UniPathwayiUPA00138.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fructose-1,6-bisphosphatase 1 (EC:3.1.3.11)
    Short name:
    FBPase 1
    Alternative name(s):
    D-fructose-1,6-bisphosphate 1-phosphohydrolase 1
    Liver FBPase
    Gene namesi
    Name:FBP1
    Synonyms:FBP
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    Proteomesi
    • UP000008227 Componenti: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi55A → L: Destabilizes the inactive T-state and promotes transition to the R-state. 1

    Chemistry databases

    ChEMBLiCHEMBL2263.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved2 Publications
    ChainiPRO_00002005002 – 338Fructose-1,6-bisphosphatase 1Add BLAST337

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylthreonine2 Publications1
    Modified residuei151N6-succinyllysineBy similarity1
    Modified residuei208Phosphoserine; by PKA1 Publication1
    Modified residuei216PhosphotyrosineBy similarity1
    Modified residuei245PhosphotyrosineBy similarity1
    Modified residuei265PhosphotyrosineBy similarity1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP00636.
    PeptideAtlasiP00636.
    PRIDEiP00636.

    PTM databases

    iPTMnetiP00636.

    Interactioni

    Subunit structurei

    Homotetramer.9 Publications

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000011671.

    Chemistry databases

    BindingDBiP00636.

    Structurei

    Secondary structure

    1338
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi14 – 24Combined sources11
    Helixi30 – 50Combined sources21
    Turni51 – 56Combined sources6
    Beta strandi59 – 64Combined sources6
    Beta strandi66 – 68Combined sources3
    Beta strandi70 – 72Combined sources3
    Helixi73 – 88Combined sources16
    Beta strandi92 – 97Combined sources6
    Beta strandi101 – 105Combined sources5
    Helixi108 – 110Combined sources3
    Beta strandi111 – 122Combined sources12
    Helixi124 – 126Combined sources3
    Turni127 – 130Combined sources4
    Beta strandi133 – 141Combined sources9
    Beta strandi144 – 146Combined sources3
    Beta strandi147 – 149Combined sources3
    Helixi150 – 153Combined sources4
    Helixi157 – 159Combined sources3
    Beta strandi161 – 178Combined sources18
    Beta strandi181 – 188Combined sources8
    Turni189 – 192Combined sources4
    Beta strandi193 – 198Combined sources6
    Beta strandi208 – 211Combined sources4
    Helixi214 – 219Combined sources6
    Helixi222 – 232Combined sources11
    Beta strandi235 – 237Combined sources3
    Beta strandi242 – 245Combined sources4
    Helixi249 – 259Combined sources11
    Beta strandi262 – 265Combined sources4
    Beta strandi268 – 270Combined sources3
    Turni271 – 273Combined sources3
    Beta strandi275 – 277Combined sources3
    Turni278 – 281Combined sources4
    Helixi282 – 291Combined sources10
    Beta strandi295 – 297Combined sources3
    Beta strandi299 – 302Combined sources4
    Helixi303 – 305Combined sources3
    Beta strandi309 – 312Combined sources4
    Beta strandi317 – 320Combined sources4
    Helixi322 – 334Combined sources13

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1CNQX-ray2.27A2-338[»]
    1EYIX-ray2.32A2-338[»]
    1EYJX-ray2.28A/B2-338[»]
    1EYKX-ray2.23A/B2-338[»]
    1FBCX-ray2.60A/B2-336[»]
    1FBDX-ray2.90A/B2-336[»]
    1FBEX-ray3.00A/B2-336[»]
    1FBFX-ray2.70A/B2-336[»]
    1FBGX-ray3.00A/B2-336[»]
    1FBHX-ray2.50A/B2-336[»]
    1FBPX-ray2.50A/B2-336[»]
    1FJ6X-ray2.50A2-338[»]
    1FJ9X-ray2.50A/B2-338[»]
    1FPBX-ray2.60A/B2-336[»]
    1FPDX-ray2.10A/B2-336[»]
    1FPEX-ray2.20A/B2-336[»]
    1FPFX-ray2.10A/B2-336[»]
    1FPGX-ray2.30A/B2-336[»]
    1FPIX-ray2.30A/B2-336[»]
    1FPJX-ray2.20A/B2-336[»]
    1FPKX-ray3.00A/B2-336[»]
    1FPLX-ray2.30A/B2-336[»]
    1FRPX-ray2.00A/B2-336[»]
    1FSAX-ray2.30A/B2-338[»]
    1KZ8X-ray2.00A/F2-338[»]
    1LEVX-ray2.15A/F2-338[»]
    1NUWX-ray1.30A2-338[»]
    1NUXX-ray1.60A2-338[»]
    1NUYX-ray1.30A2-338[»]
    1NUZX-ray1.90A2-338[»]
    1NV0X-ray1.80A2-338[»]
    1NV1X-ray1.90A2-338[»]
    1NV2X-ray2.10A2-338[»]
    1NV3X-ray2.00A2-338[»]
    1NV4X-ray1.90A2-338[»]
    1NV5X-ray1.90A2-338[»]
    1NV6X-ray2.15A2-338[»]
    1NV7X-ray2.15A/B2-338[»]
    1Q9DX-ray2.35A/B2-338[»]
    1RDXX-ray2.75A/B2-338[»]
    1RDYX-ray2.20A/B2-338[»]
    1RDZX-ray2.05A/B2-338[»]
    1YXIX-ray2.00A2-338[»]
    1YYZX-ray1.85A2-338[»]
    1YZ0X-ray2.07A/B2-338[»]
    2F3BX-ray1.80A1-338[»]
    2F3DX-ray1.83A1-338[»]
    2FBPX-ray2.80A/B2-336[»]
    2QVUX-ray1.50A/B2-338[»]
    2QVVX-ray2.03A/B2-338[»]
    3FBPX-ray2.80A/B2-336[»]
    4FBPX-ray2.50A/B/C/D2-336[»]
    4GBVX-ray2.90A2-336[»]
    4GBWX-ray2.00A2-336[»]
    4GWSX-ray2.75A/B2-338[»]
    4GWUX-ray3.00A2-338[»]
    4GWWX-ray3.20A2-338[»]
    4GWXX-ray2.35A2-338[»]
    4GWYX-ray3.00A2-338[»]
    4GWZX-ray2.60A/B2-338[»]
    4GX3X-ray2.25A/B2-338[»]
    4GX4X-ray2.50A/B2-338[»]
    4GX6X-ray2.50A/B2-338[»]
    4H45X-ray3.10A2-338[»]
    4H46X-ray2.50A2-338[»]
    4KXPX-ray2.70A/B1-338[»]
    5FBPX-ray2.10A/B2-336[»]
    ProteinModelPortaliP00636.
    SMRiP00636.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00636.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni122 – 125Substrate binding4
    Regioni213 – 216Substrate binding4
    Regioni244 – 249Substrate binding6
    Regioni275 – 277Substrate binding3

    Sequence similaritiesi

    Belongs to the FBPase class 1 family.Curated

    Phylogenomic databases

    eggNOGiKOG1458. Eukaryota.
    COG0158. LUCA.
    HOGENOMiHOG000191265.
    HOVERGENiHBG005627.
    InParanoidiP00636.
    KOiK03841.

    Family and domain databases

    CDDicd00354. FBPase. 1 hit.
    HAMAPiMF_01855. FBPase_class1. 1 hit.
    InterProiIPR000146. FBPase_class-1.
    IPR033391. FBPase_N.
    IPR028343. FBPtase.
    IPR020548. Fructose_bisphosphatase_AS.
    [Graphical view]
    PANTHERiPTHR11556. PTHR11556. 1 hit.
    PfamiPF00316. FBPase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500210. FBPtase. 1 hit.
    PIRSF000904. FBPtase_SBPase. 1 hit.
    PRINTSiPR00115. F16BPHPHTASE.
    PROSITEiPS00124. FBPASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00636-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTDQAAFDTN IVTLTRFVME EGRKARGTGE MTQLLNSLCT AVKAISTAVR
    60 70 80 90 100
    KAGIAHLYGI AGSTNVTGDQ VKKLDVLSND LVINVLKSSF ATCVLVSEED
    110 120 130 140 150
    KNAIIVEPEK RGKYVVCFDP LDGSSNIDCL VSIGTIFGIY RKNSTDEPSE
    160 170 180 190 200
    KDALQPGRNL VAAGYALYGS ATMLVLAMVN GVNCFMLDPA IGEFILVDRD
    210 220 230 240 250
    VKIKKKGSIY SINEGYAKEF DPAITEYIQR KKFPPDNSAP YGARYVGSMV
    260 270 280 290 300
    ADVHRTLVYG GIFMYPANKK SPKGKLRLLY ECNPMAYVME KAGGLATTGK
    310 320 330
    EAVLDIVPTD IHQRAPIILG SPEDVTELLE IYQKHAAK
    Length:338
    Mass (Da):36,779
    Last modified:January 23, 2007 - v4
    Checksum:i610BF8D3C6D320F6
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti2T → A AA sequence (PubMed:6291465).Curated1
    Sequence conflicti4Q → E AA sequence (PubMed:6291465).Curated1
    Sequence conflicti21E → Q AA sequence (PubMed:6296821).Curated1
    Sequence conflicti97S → T AA sequence (PubMed:6296821).Curated1
    Sequence conflicti157G → E AA sequence (PubMed:6296821).Curated1
    Sequence conflicti200D → N AA sequence (PubMed:6296821).Curated1
    Sequence conflicti229Q → E AA sequence (PubMed:6296821).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M86347 mRNA. Translation: AAA31035.1.
    PIRiS37696. PAPGF.
    RefSeqiNP_999144.1. NM_213979.1.
    UniGeneiSsc.5127.

    Genome annotation databases

    GeneIDi397038.
    KEGGissc:397038.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M86347 mRNA. Translation: AAA31035.1.
    PIRiS37696. PAPGF.
    RefSeqiNP_999144.1. NM_213979.1.
    UniGeneiSsc.5127.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1CNQX-ray2.27A2-338[»]
    1EYIX-ray2.32A2-338[»]
    1EYJX-ray2.28A/B2-338[»]
    1EYKX-ray2.23A/B2-338[»]
    1FBCX-ray2.60A/B2-336[»]
    1FBDX-ray2.90A/B2-336[»]
    1FBEX-ray3.00A/B2-336[»]
    1FBFX-ray2.70A/B2-336[»]
    1FBGX-ray3.00A/B2-336[»]
    1FBHX-ray2.50A/B2-336[»]
    1FBPX-ray2.50A/B2-336[»]
    1FJ6X-ray2.50A2-338[»]
    1FJ9X-ray2.50A/B2-338[»]
    1FPBX-ray2.60A/B2-336[»]
    1FPDX-ray2.10A/B2-336[»]
    1FPEX-ray2.20A/B2-336[»]
    1FPFX-ray2.10A/B2-336[»]
    1FPGX-ray2.30A/B2-336[»]
    1FPIX-ray2.30A/B2-336[»]
    1FPJX-ray2.20A/B2-336[»]
    1FPKX-ray3.00A/B2-336[»]
    1FPLX-ray2.30A/B2-336[»]
    1FRPX-ray2.00A/B2-336[»]
    1FSAX-ray2.30A/B2-338[»]
    1KZ8X-ray2.00A/F2-338[»]
    1LEVX-ray2.15A/F2-338[»]
    1NUWX-ray1.30A2-338[»]
    1NUXX-ray1.60A2-338[»]
    1NUYX-ray1.30A2-338[»]
    1NUZX-ray1.90A2-338[»]
    1NV0X-ray1.80A2-338[»]
    1NV1X-ray1.90A2-338[»]
    1NV2X-ray2.10A2-338[»]
    1NV3X-ray2.00A2-338[»]
    1NV4X-ray1.90A2-338[»]
    1NV5X-ray1.90A2-338[»]
    1NV6X-ray2.15A2-338[»]
    1NV7X-ray2.15A/B2-338[»]
    1Q9DX-ray2.35A/B2-338[»]
    1RDXX-ray2.75A/B2-338[»]
    1RDYX-ray2.20A/B2-338[»]
    1RDZX-ray2.05A/B2-338[»]
    1YXIX-ray2.00A2-338[»]
    1YYZX-ray1.85A2-338[»]
    1YZ0X-ray2.07A/B2-338[»]
    2F3BX-ray1.80A1-338[»]
    2F3DX-ray1.83A1-338[»]
    2FBPX-ray2.80A/B2-336[»]
    2QVUX-ray1.50A/B2-338[»]
    2QVVX-ray2.03A/B2-338[»]
    3FBPX-ray2.80A/B2-336[»]
    4FBPX-ray2.50A/B/C/D2-336[»]
    4GBVX-ray2.90A2-336[»]
    4GBWX-ray2.00A2-336[»]
    4GWSX-ray2.75A/B2-338[»]
    4GWUX-ray3.00A2-338[»]
    4GWWX-ray3.20A2-338[»]
    4GWXX-ray2.35A2-338[»]
    4GWYX-ray3.00A2-338[»]
    4GWZX-ray2.60A/B2-338[»]
    4GX3X-ray2.25A/B2-338[»]
    4GX4X-ray2.50A/B2-338[»]
    4GX6X-ray2.50A/B2-338[»]
    4H45X-ray3.10A2-338[»]
    4H46X-ray2.50A2-338[»]
    4KXPX-ray2.70A/B1-338[»]
    5FBPX-ray2.10A/B2-336[»]
    ProteinModelPortaliP00636.
    SMRiP00636.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000011671.

    Chemistry databases

    BindingDBiP00636.
    ChEMBLiCHEMBL2263.

    PTM databases

    iPTMnetiP00636.

    Proteomic databases

    PaxDbiP00636.
    PeptideAtlasiP00636.
    PRIDEiP00636.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi397038.
    KEGGissc:397038.

    Organism-specific databases

    CTDi2203.

    Phylogenomic databases

    eggNOGiKOG1458. Eukaryota.
    COG0158. LUCA.
    HOGENOMiHOG000191265.
    HOVERGENiHBG005627.
    InParanoidiP00636.
    KOiK03841.

    Enzyme and pathway databases

    UniPathwayiUPA00138.
    BRENDAi3.1.3.11. 6170.
    SABIO-RKP00636.

    Miscellaneous databases

    EvolutionaryTraceiP00636.
    PROiP00636.

    Family and domain databases

    CDDicd00354. FBPase. 1 hit.
    HAMAPiMF_01855. FBPase_class1. 1 hit.
    InterProiIPR000146. FBPase_class-1.
    IPR033391. FBPase_N.
    IPR028343. FBPtase.
    IPR020548. Fructose_bisphosphatase_AS.
    [Graphical view]
    PANTHERiPTHR11556. PTHR11556. 1 hit.
    PfamiPF00316. FBPase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500210. FBPtase. 1 hit.
    PIRSF000904. FBPtase_SBPase. 1 hit.
    PRINTSiPR00115. F16BPHPHTASE.
    PROSITEiPS00124. FBPASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiF16P1_PIG
    AccessioniPrimary (citable) accession number: P00636
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: November 2, 2016
    This is version 151 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The molecule has a highly reactive cysteine residue (Cys-117 or Cys-129), which tends to form mixed disulfides (e.g. with homocystine) but is not essential for enzyme activity.

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.